Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Nuclear localization sequence of FUS and induction of stress granules by ALS mutants.

Neurobiology of aging - 1 Dec 2011

Gal Jozsef, Zhang Jiayu, Kwinter David M, Zhai Jianjun, Jia Hongge, Jia Jianhang, Zhu Haining

Abstract excerpt

Mutations in fused in sarcoma (FUS) have been reported to cause a subset of familial amyotrophic lateral sclerosis (ALS) cases. Wild-type FUS is mostly localized in the nuclei of neurons, but the ALS mutants are partly mislocalized in the cytoplasm and can form inclusions. We demonstrate that the C-terminal 32 amino acid residues of FUS constitute an effective nuclear localization sequence (NLS) as it targeted...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyotrophic Lateral Sclerosis
Share to Cytoplasmic Granules

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Inclusion Bodies

Share to Motor Neurons

Share to Nuclear Localization Signals

Share to Oxidative Stress

Share to RNA-Binding Protein FUS

Source

Open in PubMed Open full text

Identifiers

PMID: 20674093
DOI: 10.1016/j.neurobiolaging.2010.06.010
PMCID: PMC2997923

Genes

FUS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nuclear localization sequence of FUS and induction of stress granules by ALS mutants.PMID 20674093Read ↗

ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules.Semantic proximity Read ↗

ALS-linked cytoplasmic FUS assemblies are compositionally different from physiological stress granules and sequester hnRNPA3, a novel modifier of FUS toxicity.Semantic proximity Read ↗

Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granulesSemantic proximity Read ↗

Nuclear transport impairment of amyotrophic lateral sclerosis‐linked mutations in FUS/TLSSemantic proximity Read ↗

Compositional analysis of ALS-linked stress granule-like structures reveals factors and cellular pathways dysregulated by mutant FUS under stressSemantic proximity Read ↗

Subcellular localization and RNAs determine FUS architecture in different cellular compartments.Semantic proximity Read ↗

RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutationsSemantic proximity Read ↗

Self-assembled FUS binds active chromatin and regulates gene transcription.Semantic proximity Read ↗

Aggregation of ALS-linked FUS mutant sequesters RNA binding proteins and impairs RNA granules formation.Semantic proximity Read ↗

Amyotrophic Lateral Sclerosis, FUS and Protein Synthesis Defects.Semantic proximity Read ↗

Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons.Semantic proximity Read ↗

RNA Binding Protein TAF15 Suppresses Toxicity in a Yeast Model of FUS ProteinopathySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.